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The patatin-like protein PlpD forms novel structurally dynamic homodimers in the Pseudomonas aeruginosa outer

Sarah E Hanson1, Matthew Thomas Doyle1, Harris D Bernstein1

  • 1Genetics and Biochemistry Branch, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 USA.

Biorxiv : the Preprint Server for Biology
|June 19, 2023
PubMed

Insights

Pseudomonas aeruginosa PlpD, an outer membrane protein, challenges existing models by localizing its N-terminal domain to the periplasm and forming a homodimer. This protein exhibits unique structural dynamics, expanding the known functions of the Omp85 superfamily.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • The Omp85 superfamily comprises outer membrane proteins (OMPs) crucial for protein transport in bacteria, mitochondria, and chloroplasts.
  • These proteins typically feature a β-barrel domain and POTRA domains, facilitating OMP assembly and translocation.
  • Pseudomonas aeruginosa PlpD represents a distinct Omp85 family member with a putative N-terminal patatin-like (PL) domain.

Approach:

  • Investigated the localization and quaternary structure of Pseudomonas aeruginosa PlpD.
  • Utilized structural biology techniques to analyze the dynamic interactions within the PlpD protein.
  • Challenged established models of Omp85 protein function and translocation.

Key Points:

  • Contrary to expectations, the PlpD PL-domain is exclusively located in the periplasm.
  • PlpD forms a homodimer, a characteristic not observed in previously studied Omp85 proteins.
  • A unique dynamic segment within the PL-domain undergoes transient strand-swapping with the β-barrel domain.

Conclusions:

  • The Omp85 superfamily exhibits greater structural diversity than previously understood.
  • The Omp85 scaffold has been evolutionarily adapted to support novel protein functions.
  • PlpD's unique structure and localization suggest new mechanisms for outer membrane protein regulation.
Keywords:
Omp85 superfamilyPseudomonas aeruginosabacterial outer membranemembrane proteinsprotein folding

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